H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH combines basic, acidic, hydrophobic, and aromatic residues that generate a diverse interaction landscape. Researchers study its hydrogen-bond tendencies and folding in aqueous systems. Charge distribution influences binding and structural adaptability. Applications include motif mapping, peptide engineering, and biophysical evaluation.
CAT No: R2633
CAS No:146877-90-9
Synonyms/Alias:CMX-8933;EX-A9705;HY-P10506;CS-1102380;146877-90-9;
H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH, also known as a custom synthetic octapeptide, is a specialized peptide sequence composed of lysine, glutamic acid, threonine, leucine, glutamine, phenylalanine, and arginine residues. This octapeptide is designed for advanced research applications, offering a precise arrangement of amino acids that can mimic or modulate biological processes. Its unique structure imparts distinct physicochemical properties, making it suitable for a range of scientific investigations. With its versatility and compatibility with various biochemical assays, this compound serves as a valuable tool for researchers exploring peptide interactions, signaling pathways, and molecular recognition events. The presence of both hydrophilic and hydrophobic amino acids enables it to participate in diverse experimental settings, supporting studies that require targeted peptide design and functional analysis.
Peptide-Protein Interaction Studies: H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH is frequently utilized in peptide-protein interaction assays to elucidate binding mechanisms and affinity profiles. By incorporating this sequence into binding studies, researchers can investigate the specific recognition patterns between the octapeptide and target proteins, aiding in the identification of potential binding motifs and functional domains. Such insights are critical for understanding protein function, mapping interaction networks, and designing peptide-based inhibitors or modulators for further research applications.
Enzyme Substrate Analysis: As a synthetic substrate, the octapeptide can be employed to assess the activity and specificity of proteolytic enzymes. Researchers can introduce the peptide into enzymatic assays to monitor cleavage events, determine substrate preferences, and characterize enzyme kinetics. The sequence diversity within H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH allows for detailed analysis of enzyme-substrate interactions, supporting the development of novel assays for protease identification, inhibitor screening, and mechanistic studies of enzymatic processes.
Signal Transduction Research: The peptide serves as a model system for dissecting cellular signaling pathways. By incorporating the octapeptide into cell-based assays or in vitro signaling studies, scientists can probe the effects of specific amino acid sequences on signal transduction events. This approach facilitates the identification of key regulatory motifs, the mapping of post-translational modification sites, and the exploration of downstream cellular responses, thereby advancing the understanding of complex signaling networks.
Structural Biology Investigations: H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH is valuable for structural biology research, where it can be used to study peptide folding, conformational dynamics, and secondary structure formation. Techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and X-ray crystallography benefit from the defined sequence and chemical properties of the peptide. These studies contribute to elucidating the structural determinants of peptide function, guiding the rational design of peptides with tailored biological activities.
Peptide-Based Material Science: The octapeptide finds application in the development of peptide-based materials, including hydrogels, nanostructures, and surface coatings. Its balanced composition of charged and hydrophobic residues enables self-assembly and interaction with various substrates, making it suitable for fabricating functional biomaterials. Researchers leverage these properties to create novel materials for biosensing, drug delivery, and tissue engineering, expanding the utility of peptides beyond traditional biochemical research.
Bioanalytical Method Development: H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH supports the advancement of bioanalytical techniques by serving as a standard or probe in mass spectrometry, chromatography, and immunoassay platforms. Its well-defined sequence and stability facilitate method validation, calibration, and optimization of detection protocols. By providing a reliable reference compound, the peptide enhances the accuracy and reproducibility of quantitative analyses, enabling robust measurement of peptides and proteins in complex biological samples. Through these diverse applications, this octapeptide demonstrates its significance as a multifunctional reagent in modern biochemical and biotechnological research.
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